Cycloamyloses mimic enzyme action. In pursuit of our overall aim to detail the structural aspects of the binding of phenyl esters to cycloheptaamylose and the mechanism of their hydrolysis catalyzled by cycloheptammylose, complexes of cycloheptaamylose with inhibitor and substrate analogues will be determined using X-ray diffraction methods. These include the complexes with adamantane carboxylic acid, 1-adamantylpropiolic acid (or amide), 3-6-butyl-1-adamantylpropiolic acid (or amide) and ferrocene carbolxylic acid. The structure of complexes of the 'capped' cycloheptaamylose (the hepta-N-methyl formamide derivative) will also be examined to try to define the effect of 'capping' on the substrate or inhibitor binding. The ionophores are useful tools for research as well as models for membrane transport. Molecular structures of certain antibiotics with and without the complexed ions will be determined by X-ray diffraction methods. These include enniatin B with several different ions, beauvericin rubidium picrate, valinomycin picrate and those uncomplexed and complexed structures necessary to complete the series valinomycin, PV-Lac and prolinomycin. These will be compared and the structural information correlated with the already published membrane studies.